1a7h

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Current revision (05:54, 3 April 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1a7h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7H FirstGlance]. <br>
<table><tr><td colspan='2'>[[1a7h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7H FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7h OCA], [https://pdbe.org/1a7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7h RCSB], [https://www.ebi.ac.uk/pdbsum/1a7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7h ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.56&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7h OCA], [https://pdbe.org/1a7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7h RCSB], [https://www.ebi.ac.uk/pdbsum/1a7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7h ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a7h ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The 2-domain gammaS-crystallin, a highly conserved early evolutionary off-shoot of the gamma-crystallin family, is located in the water-rich region of eye lenses. The expressed C-terminal domain, gammaS-C, has been crystallized and the 2.56 A X-ray structure determined. There are two domains in the asymmetric unit which pair about a distorted twofold axis. One of the domains has an altered conformation in a highly conserved region of the protein, the tyrosine corner. The distorted gammaS-C dimer of domains is compared with the highly symmetrical, equivalent recombinant dimer of C-terminal domains from gammaB-crystallin. Sequence changes close to the interface, that distinguish gammaS from the other gamma-crystallins, are examined in order to evaluate their role in symmetrical domain pairing.
 
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The C-terminal domains of gammaS-crystallin pair about a distorted twofold axis.,Basak AK, Kroone RC, Lubsen NH, Naylor CE, Jaenicke R, Slingsby C Protein Eng. 1998 May;11(5):337-44. PMID:9681865<ref>PMID:9681865</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1a7h" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Crystallin 3D structures|Crystallin 3D structures]]
*[[Crystallin 3D structures|Crystallin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

GAMMA S CRYSTALLIN C-TERMINAL DOMAIN

PDB ID 1a7h

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